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PSGL1 and Siglec-5 are in close proximity at the leukocyte surface.SPSGL1 is a ligand for Siglec-5 and interacts with Siglec-5 ectodomain.Siglec-5 plays a role in PSGL1-mediated leukocyte rolling and the inflammatory response in general.
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An unbiased screen revealed Hsp70 as a ligand for Siglec-5 and Siglec-14. Hsp70 stimulation through Siglec-5 delivers an anti-inflammatory signal, while stimulation through Siglec-14 is pro-inflammatory.
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Data indicate that the Siglec-5/14 genotype influences neutrophil responses to group B Streptococcus.
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we found that secretory IgA is taken up by M cells via the Dectin-1 receptor, with the possible involvement of Siglec-5 acting as a co-receptor.
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These studies demonstrate the Siglec5 carbohydrate recognition domain alone is sufficient for binding sialylated carbohydrates and provide a foundation for further investigation of Siglec5 structure and function.
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Siglec-5 expression protects T cells from HIV-1- and apoptosis-induced cell death and contributes to the different outcomes of HIV-1 infection in humans and chimpanzees.
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Human Siglec-5 inhibitory receptor and immunoglobulin A (IgA) have separate binding sites in streptococcal beta protein.
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Siglec-5 expression correlates with lack of proliferation in a subset of human cells, and is upregulated by activation of chimpanzee but not human lymphocytes.
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expression of Siglec-5 on cells of the myelomonocytic lineage and alteration of its expression by inflammatory stimuli suggest a role for this protein in cell/cell interactions following microbial exposure.
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Siglec-5 can be classified as an inhibitory receptor with the potential to mediate SHP-1 and/or SHP-2-dependent signaling in the absence of tyrosine phosphorylation.
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Siglecs-5 did not interact with sulfate derivatives of LacNAc and sulfated oligosaccharides containing sialic acid.
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The expression levels of Siglec-5 were high or detectable in bone marrow plasma from AML patients and serum from normal donors.
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Siglec-14 and Siglec-5 appear to be the first glycan binding paired receptors. Near-complete sequence identity of the amino-terminal part of human Siglec-14 and Siglec-5 indicates partial gene conversion between SIGLEC14 and SIGLEC5.
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Siglec-5 is identified as a receptor for alpha-1-acid glycoprotein (AGP) 1 in human neutrophils.
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Structural implications of SIGLEC5-mediated sialoglycan recognition are reported.
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Group B Streptococcus beta protein binding to Siglec-5 functions to impair leukocyte phagocytosis, oxidative burst, and extracellular trap production, promoting bacterial survival.
